Hydroxylamine-stable covalent linkage of myristic acid in G0 alpha, a guanine nucleotide-binding protein of bovine brain
Schultz, A.M.; Tsai, S.C.; Kung, H.F.; Oroszlan, S.; Moss, J.; Vaughan, M.
Biochemical and Biophysical Research Communications 146(3): 1234-1239
1987
ISSN/ISBN: 0006-291X PMID: 3113429 Document Number: 301539
Go .alpha., a guanine nucleotide-binding protein with a strong homology to the G1 .alpha. and Gs .alpha. regulatory proteins of adenylate cyclase, is shown to contain myristic acid. The attachment of myristate to the protein is stable to hydroxylamine treatment, and since the amino-terminal sequence of Go .alpha. is typical of proteins with amino-terminal myristate, the inference is strong that Go .alpha. is also myristylated at its amino-terminal glycine.